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Study of the interaction between N-confused porphyrin and bovine serum albumin by fluorescence spectroscopy by Xianyong Yu; Ronghua Liu; Rongqiong Yi; Fengxian Yang; Haowen Huang; Jian Chen; Danhong Ji; Ying Yang; Xiaofang Li; Pinggui Yi is a Chemistry article available to read on EtoBox.

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The fluorescence and ultraviolet spectroscopy were explored to study the interaction between Nconfused porphyrins (NCP) and bovine serum albumin (BSA) under imitated physiological condition. The experimental results indicated that the fluorescence quenching mechanism between BSA and NCP was static quenching procedure at low NCP concentration at 293 and 305 K or a combined quenching (static and dynamic) procedure at higher NCP concentration at 305 K. The binding constants, binding sites and the corresponding thermodynamic parameters H, S, and G were calculated at different temperatures. The comparison of binding potency of the three NCP to BSA showed that the substituting groups in benzene ring could enhance the binding affinity. From the thermodynamic parameters, we concluded that the action force was mainly hydrophobic interaction. The binding distances between NCP and BSA were calculated using Förster non-radiation energy transfer theory. In addition, the effect of NCP on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.

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Author

Xianyong Yu; Ronghua Liu; Rongqiong Yi; Fengxian Yang; Haowen Huang; Jian Chen; Danhong Ji; Ying Yang; Xiaofang Li; Pinggui Yi

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Pergamon Press Ltd.; Elsevier BV (ISSN 1386-1425)

Published

2011

Language

EN

Field

Chemistry (Physical Sciences)